ATP-diphosphohydrolases, apyrases, and nucleotide phosphohydrolases. Biochemical properties and functions

Biomembranes: A Multi-Volume Treatise

Volumn 5, Issue C, 1996, Pages 369-401

  Beaudoin, Adrien R ^a   Sévigny, Jean ^a   Picher, Maryse ^a  

^a UNIVERSITÉ DE SHERBROOKE   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 77957057275     PISSN: 18745342     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1874-5342(06)80015-2     Document Type: Review

References (216)

1. Agren G., Ponten J., Ronquist G., and Westmark B. Demonstration of an ATPase at the cell surface of intact normal and neoplastic tumor cells in culture. J. Cell. Physiol. 78 (1971) 171-176
2. Alertsen A.R., Walaas O., and Walass E. Enzymic conversion of mononucleotides by rat diaphragm. Acta Physiol. Scand. 43 (1958) 122-134
3. Anich M., Fanta N., Mancilla M., Kettlun A.M., Valenzuela M.A., and Traverso-Cori A. Apyrase activity and changes in metabolites during germination and tuberization of Solanum tuberosum. Phytochemistry 29 (1990) 1411-1415
4. Bach M.K. Mediators of anaphylaxis and inflammation. Ann. Rev. Microbiol. 36 (1982) 371-413
5. Baer H.P., and Drummond G.I. Catabolism of adenine nucleotides by the isolated perfused rat heart. Proc. Soc. Exp. Biol. Med. 127 (1968) 33-36
6. Battastini A.J., Da Rocha J.B., Barcellos C.K., Dias R.D., and Sarkis J.J. Characterization of an ATP diphosphohydrolase (EC 3.6.1.5) in synaptosomes from cerebral cortex of adult rats. Neurochem. Res. 16 (1991) 1303-1310
7. Beaudoin A.R., and Grondin G. Shedding of vesicular material from the cell surface of eukaryotic cells: Different cellular phenomena. Biochim. Biophys. Acta 1071 (1991) 203-219
8. Beaudoin A.R., Laliberté J.-F., LeBel D., Lord A., Grondin G., Phaneuf S., and St-Jean P. Localization and physiological role of the ATP-diphosphohydrolase in the pancreatic acinal cell. In: Ribet A., Pradayrol L., and Susini C. (Eds). Biology of Normal and Cancerous Exocrine Pancreatic Cells. INSERM Symposium No. 15 (1980), Elsevier, North Holland Press, New York 273-280
9. Beaudoin A.R., Vachereau A., Grondin G., Rosenberg M.D., and Strobel R. Microvesicular secretion, a mode of cell secretion associated with the presence of an ATP-diphosphohydrolase. FEBS Lett. 203 (1986) 1-2
10. Belardinelli L., Shryock J., West G.A., Clemo H.F., Dimarco J.P., and Berne R.M. Effects of adenosine and adenine nucleotides on the atrioventricular node of isolated guinea pig hearts. Circulation 70 (1984) 1083-1091
11. Berger S.J., and Sacktor B. Isolation and biochemical characterization of brush borders from rabbit kidney. J. Cell Biol. 47 (1970) 637-645
12. Bonner J., and Vanner J.E. Plant Biochemistry. 3rd Ed. (1976), Academic Press
13. Bowditch J., Nigdikar S., Brown A.K., and Dow J.W. 5′-nucleotidase activity of isolated mature rat cardiac myocytes. Biochim. Biophys. Acta 845 (1985) 21-26
14. Burnstock G. Physiological and pathological roles of purines: An update. Drug. Dev. Res. 28 (1993) 195-206
15. 291-40P. Carleton J.S., Gordon J.L., Hutchings A., and Pearson J.D. Secretion and extracellular metabolism of adenine nucleotides by endothelial cells in culture. J. Physiol. (London) (1979)
16. Chakravarty N., and Echetebu Z. Plasma membrane adenosine triphosphatases in rat mast cells and macrophages: the relation of the mast cell enzyme to histamine release. Biochem. Pharmacol. 27 (1978) 1561
17. 2+-activated adenosine triphosphatase in plasma and granule membranes in non-secreting and secreting mast cells. An electron microscopic histochemical study. Exper. Cell Res. 130 (1980) 175-184
18. Chelliah R., and Bakhle Y.S. The fate of adenine nucleotides in the pulmonary circulation of isolated lung. Q. J. Exp. Physiol. 68 (1983) 289-300
19. 2+-ATPase from rat parotid gland plasma membranes has the characteristics of an ecto-ATPase. Cell. Sign. 4 (1992) 25-35
20. Cohn M., and Meek G.A. The mechanism of hydrolysis of adenosine di- and triphosphate catalysed by potato apyrase. Biochem. J. 66 (1957) 128-132
21. Cooper D.R., Lewis G.P., Lieberman G.E., Webb H., and Westwick J. ADP metabolism in vascular tissue, a possible thrombo-regulatory mechanism. Thromb. Res. 14 (1979) 901-914
22. Cooper P.H., and Stanworth D.R. Effect of removal of calcium-activated adenosine triphosphatase from rat mast cells by treatment with sodium glycocholate. Biochem. J. 168 (1977) 583-585
23. Cori O., Traverso-Cori A., Tetas M., and Chaimovich H. Substrate specificity and inhibition studies on potato apyrase. Biochem. Z. 342 (1965) 345-358
24. Côté Y.P., Picher M., St-Jean P., Béliveau R., Potier M., and Beaudoin A.R. Identification and localization of ATP-diphosphohydrolase (apyrase) in bovine aorta: Relevance to vascular tone and platelet aggregation. Biochim. Biophys. Acta 1978 (1991) 187-191
25. Côté Y.P., Filep J.G., Battistini B., Gauvreau J., Sirois P., and Beaudoin A.R. Characterization of ATP-diphosphohydrolase activities in the intima and media of the bovine aorta: evidence for a regulatory role in platelet activation in vitro. Biochim. Biophys. Acta 1139 (1992) 133-142
26. Côté Y.P., Ouellet S., and Beaudoin A.R. Kinetic properties of type-II ATP diphosphohydrolase from the tunica media of the bovine aorta. Biochim. Biophys. Acta 1160 (1992) 246-250
27. Coutts A.A., Jorrizo J.L., Eady R.A.J., Greaves M.W., and Burnstock G. Adenosine triphosphate-evoked vascular changes in human skin: Mechanism of action. Eur. J. Pharmacol. 76 (1981) 391-401
28. Crutchley D.J., Eling E.E., and Anderson M.W. ADPase activity of isolated perfused rat lung. Life Sci. 22 (1978) 1413-1420
29. Culic O., Sabolic I., and Zanic-Grubisic T. The stepwise hydrolysis of adenine nucleotides by ectoenzymes of rat renal brush-border membranes. Biochim. Biophys. Acta 1030 (1990) 143-151
30. Curdova E., Jechova V., and Hostalek Z. Properties of apyrase and inorganic pyrophosphatase in Streptomyces aurofaciens. Folia Microbiol. 27 (1982) 159-166
31. Cusack N.J., and Hourani S.M.O. Some pharmacological and biochemical interactions of the enantiomers of adenylyl 5′-(β,γ-methylene)-diphosphonate with the guinea-pig urinary bladder. Br. J. Pharmacol. 82 (1984) 155-160
32. Damiani E., Margreth A., Furlan A., Dahms A.S., Arnn J., and Sabbadini R.A. Common structural domains in the sarcoplasmic reticulum calcium ATPase and the transverse tubule magnesium-ATPase. J. Cell. Biol. 104 (1987) 461-472
33. De Vente J., Velema J., and Zaagsma J. Properties and subcellular localization of adenosine diphosphatase in rat heart. Arch. Biochem. Biophys. 233 (1984) 180-187
34. Del Campo G., Puente J., Valenzuela M.A., Traverso-Cori A., and Cori O. Hydrolysis of synthetic pyrophosphoric esters by an isoenzyme of apyrase from Solanum tuberosum. Biochem. J. 167 (1977) 525-529
35. DePierre J.W., and Karnowsky M.I. Ectoenzymes of the guinea-pig polymorphonuclear leukocyte. I. Evidence for an ecto-adenosine monophosphatase, -adenosine triphosphatase, and -p-glycerophenylphosphatase. J. Biol. Chem. 249 (1974) 7111-7120
36. DePierre J.W., and Karnowsky M.L. Ecto-enzymes of the guinea-pig polymorphonuclear leukocyte. II. Properties and suitability as marker for the plasma membrane. J. Biol. Chem. 249 (1974) 7121-7129
37. Dieterle Y., Ody C., Ehrensberger A., Stalder H., and Junod A.F. Metabolism and uptake of adenosine triphosphate and adenosine by porcine aortic and pulmonary endothelial cells and fibroblasts in culture. Circ. Res. 42 (1978) 869-876
38. Dombrowski K.E., Trevillyan J.M., Cone J.C., Lu Y., and Phillips C.A. Identification and partial characterization of an ectoATPase expressed by human natural killer cells. Biochemistry 32 (1993) 6515-6522
39. 2+-dépendante des membranes plasmiques de lymphocytes. Effet de la concanavaline A sur les ATPases membranaires. Biochimie (Paris) 56 (1974) 851-857
40. Dornand J., Bonnafous J.C., Gartner A., Favero J., and Mani J.C. Sudy of ecto-5′-nucleotidase, ecto-ATPase, and adenosine deaminase activities in relation to lymphoid cell differentiation. In: Kreutzberg, et al. (Ed). Cellular Biology of Ectoenzymes (1986), Springer-Verlag, New York 72-85
41. Dosne A.M., Legrand C., Bauvois B., Bodevin E., and Caen J.P. Comparative degradation of adenylnucleotides by cultured endothelial cells and fibroblasts. Biochem. Biophys. Res. Commun. 85 (1978) 183-189
42. Dunkley C.R., Manery J.F., and Dryden E.E. The conversion of ATP to IMP by muscle surface enzymes. J. Cell Physiol. 68 (1966) 241-248
43. Edwards F.A., Gibb A.J., and Colquhoun D. ATP receptor-mediated synaptic currents in the central nervous system. Nature 359 (1992) 144-147
44. El-Moatassim C., Dornand J., and Mani J.-C. Extracellular ATP and cell signalling. Biochim. Biophys. Acta 1134 (1992) 31-45
45. Emmelot P., Bos E.L., Benedetti E.L., and Rumke P. Studies on plasma membranes. I. Chemical composition and enzyme content of plasma membranes isolated from rat liver. Biochim. Biophys. Acta 90 (1964) 126-145
46. th Colloquium Bruges, Vol. 15 (1968), Elsevier, Berlin, Heidelberg
47. Engelhardt W.A. Enzymes as structural elements of physiological mechanisms. Proc. Int. Symp. Enzyme Chem. (Tokyo and Kyoto) 2 (1957) 163-166
48. 2+-ATPase in the plasma membrane of rat myometrium. Biochem. J. 252 (1988) 215-220
49. Ernster L., and Jones L.C. A study of nucleoside tri- and diphosphate activities of rat liver microsomes. J. Cell Biol. 15 (1962) 563-578
50. Evans R.J., Derkach V., and Surprenant A. ATP-mediated fast synaptic transmission in mammalian neurons. Nature 357 (1992) 503-505
51. Filippini A., Taffs R.E., Agui T., and Sitkovsky M.V. Ecto-ATPase activity in cytolytic T-lymphocytes. Protection from the cytolytic effects of extracellular ATP. J. Biol. Chem. 265 (1990) 334-340
52. Fiske C.H., and Subbarow Y. The colorimetric determination of phosphorus. J. Biol. Chem. 66 (1925) 375-400
53. Fleetwood G., Coade S.B., Gordon J.L., and Pearson J.D. Kinetics of adenine nucleotide catabolism in the coronary circulation of rats. Am. J. Physiol. 256 (1989) H1565-H1572
54. Ford-Hutchinson A.W. Aggregation of rat neutrophils by nucleotide triphosphates. Br. J. Pharmacol. 76 (1982) 467-471
55. Gantzer M.L., and Grisham C.M. Characterization of magnesium-ATPase from sheep kidney medulla: Purification. Arch. Biochem. Biophys. 198 (1979) 263-267
56. Glasgow J.G., Schade R., and Pitlick F.A. Evidence that ADP hydrolysis by human cells is related to thrombogenic potential. Thromb. Res. 13 (1978) 255-266
57. Gordon E.L., Pearson J.D., and Slakey L.L. The hydrolysis of extracellular adenine nucleotides by cultured endothelial cells from pig aorta. Free-foward inhibition of adenosine production at the cell surface. J. Biol. Chem. 261 (1986) 15496-15504
58. Gordon E.L., Pearson J.D., Dickinson E.S., Moreau D., and Slakey L.L. The hydrolysis of extracellular adenine nucleotides by arterial smooth muscle cells. Regulation of adenosine production at the cell surface. J. Biol. Chem. 264 (1989) 18986-18992
59. Grantham C.J., and Bakhle Y.S. Effect of acute lung injury on metabolism of adenine nucleotides in rat perfused lung. Br. J. Pharmacol. 94 (1988) 1029-1036
60. Guranowski A., Starzynska E., Rataj-Guranowska M., and Gunther Sillero M.A. Purification of apyrase from yellow Lupin cotyledons after extraction with perchloric acid. Prot. Exp. Purif. 2 (1991) 235-239
61. +)-dependent ATPase in the salivary glands and intestinal mucosa. Biochim. Biophys. Acta 304 (1973) 533-540
62. Habliston D.L., Ryan U.S., and Ryan J.W. Endothelial cells degrade adenosine-5′-diphosphate. J. Cell. Biol. 79 (1978) 206A
63. Hellewell P.G., and Pearson J.D. Nucleotides and pulmonary endothelium. In: Ryan U.S. (Ed). Pulmonary Endothelium in Health and Disease (1987) 327-348
64. Heyns A.d.P., Van den Berg D.J., Potgieter G.M., and Retief F.P. The inhibition of platelet aggregation by an aorta intima extract. Thrombos. Diathes. Haemorrh. 32 (1974) 417-431
65. 2+-ATPase of transverse tubule membranes isolated from rabbit skeletal muscles. J. Biol. Chem. 258 (1983) 13937-13945
66. Horgan D.J., and Kuypers R. Biochemical properties of purified transverse tubules isolated from skeletal muscle triads. Arch. Biochem. Biophys. 260 (1988) 1-9
67. Hulstaert C.E., Kalicharan D., Poelstra K., Bakker W.W., and Hardonk M.J. Survey of the occurrence of adenosine polyphosphatase in extracellular matrix of rat tissues. A cytochemical investigation. Histochemistry 96 (1991) 441-447
68. Ishikawa H., Tamiya T., Tsuchiya T., and Matsumoto J.J. A novel ATP-ADPase from Mimosa pulvinus. Comp. Biochem. Physiol. 78B (1984) 59-61
69. Jechova V., Curdova E., and Hostalek Z. Role of phosphatase in the biosynthesis of chlortetracycline in Streptomyces aureofaciens. Folia Microbiol 27 (1982) 153-158
70. Juul B., Lüscher M.E., Aalkjaer C., and Plesner L. Nucleotide hydrolytic activity of isolated intact rat mesenteric small arteries. Biochim. Biophys. Acta 1067 (1991) 201-207
71. Kalckar H.M. Adenylpyrophosphatase and myokinase. J. Biol. Chem. 153 (1944) 355-367
72. Keller F., and Zimmermann H. Ecto-adenosine triphosphatase activity at the cholinergic nerve endings of the Torpedo electric organ. Life Sci. 33 (1983) 2635-2641
73. Kettlun A.M., Uribe L., Silva S., Rivera J., Valenzuela M.A., and Traverso-Cori A. Chemical modification of aromatic acid and basic amino-acids of 2 isoenzymes of apyrase EC-3.6.1.5. from Solanum tuberosum. Arch. Biol. Med. Exp. 14 (1981) 171-176
74. Kettlun A.M., Uribe L., Calvo V., Silva S., Rivera J., Mancilla M., Valenzuela M.A., and Traverso-Cori A. Properties of two apyrases from Solanum tuberosum. Phytochemistry 21 (1982) 551-558
75. Kiessling K.H. Studies on thiamine triphosphate. Biochim. Biophys. Acta 20 (1956) 293-298
76. Kinne-Saffran E., and Kinne R. Localization of a calcium-stimulated ATPase in the basal-lateral plasma membranes of the proximal tubule of rat kidney cortex. J. Membr. Biol. 17 (1974) 263-274
77. 2+-ATPase from rabbit skeletal muscle transverse tubule. J. Biol. Chem. 263 (1988) 12682-12689
78. 2+)-ATPase from the plasma membranes of a human oat cell carcinoma. J. Biol. Chem. 259 (1984) 10919-10924
79. Knowles A.F., Isler R.E., and Reece J.F. The common occurrence of ATP diphosphohydrolase in mammalian plasma membranes. Biochim. Biophys. Acta 731 (1983) 88-96
80. Kragballe K., and Ellegaard J. ATPase activity of purified human normal T-and B-lymphocytes. Scand. J. Haematol. 20 (1978) 271-279
81. Krishnan P.S. Studies on apyrases. I. Purification of potato apyrase by fractional precipitation with ammonium sulfate. Arch. Biochem. 20 (1949) 261-271
82. Krishnan P.S. Studies on apyrase. II. Some properties of potato apyrase. Arch. Biochem. 20 (1949) 272-283
83. Kuhn N.J., and White A. The role of nucleoside diphosphatase in a uridine nucleotide cycle associated with lactose synthesis in rat mammary-gland Golgi apparatus. Biochem. J. 168 (1977) 423-433
84. Kwan C.Y., and Ramlal T. On the inhibition of smooth muscle membrane ATPase by sodium azide. Biochem. Intern. 4 (1982) 439-449
85. Kwan C.-Y., Lee R.M.K.W., and Daniel E.E. Isolation of plasma membranes from mesenteric veins: A comparison of their physical and biochemical properties with arterial membranes. Blood Vessels 18 (1981) 171-186
86. Kwan C.-Y., Sakai Y., Grover A.K., and Lee R.M.L.W. Isolation and characterization of plasma membrane fraction from gastric fundus smooth muscle of the rat. Mol. Physiol. 2 (1982) 107-120
87. Kwan C.-Y., Triggle C.R., Grover A.K., Lee R.M.K.W., Ramlal T., and Daniel E.E. Canine aortic microsomes: Isolation and characterization. Can. Fed. Proc. 25 (1982) 98
88. Kwan C.-Y., Lee R.M.K.W., and Grover A.K. Isolation and characterization of plasma membrane fraction from gastric fundus smooth muscle of the rat. Mol. Physiol. 2 (1983) 107-120
89. Kwan C.-Y., Triggle C.R., Grover A.K., Lee R.M.K.W., and Daniel E.E. An analytical approach to the preparation and characterization of subcellular membranes from canine mesenteric arteries. Prep. Biochem. 13 (1983) 275-314
90. Kwan C.-Y., Kostka P., and Ramlal T. Properties of a widespread azide-sensitive adenosine diphosphohydrolase in smooth muscle. Molec. Physiol. 6 (1984) 99-114
91. Laliberté J.-F., and Beaudoin A.R. Sequential hydrolysis of the γ and β-phosphate groups of ATP by the ATP diphosphohydrolase from pig pancreas. Biochim. Biophys. Acta 742 (1983) 9-15
92. 2+ on ATP hydrolysis by the purified ATP-diphosphohydrolase. J. Biol. Chem. 257 (1982) 3869-3874
93. LeBel D., Poirier G.G., Phaneuf S., St-Jean P., Laliberté J.-F., and Beaudoin A.R. Characterization and purification of a calcium-sensitive ATP diphosphohydrolase from pig pancreas. J. Biol. Chem. 255 (1980) 1227-1233
94. Lee K.H., and Eiler J.J. Temperature-dependent characteristics of an adenylpyrophosphatase preparation from potatoes. Science 114 (1951) 393-395
95. Liébecq C., Lallemand A., and Degueldre-Guillaume M.J. The apyrase activity of potato extract. Arch. Biochem. Biophys. 97 (1962) 609-610
96. Liébecq C., Lallemand A., and Degueldre-Guillaume M.J. Purification partielle et propriétés de l'apyrase de la pomme de terre. Bull. Soc. Chim. Biol. 45 (1963) 573-594
97. Lieberman G.E., and Lewis G.P. Properties of vascular ADPase. Artery 8 (1980) 374-380
98. Lieberman G.E., Leake D.S., and Peters T.J. Subcellular localization of adenosine diphosphatase in cultured pig arterial endothelial cells. Thromb. Haemostas. (Stittgart) 47 (1982) 249-253
99. 2+)-ATPase is not a calcium pump. Comparison with ATP-dependent calcium transporter. J. Biol. Chem. 260 (1985) 10976-10980
100. 2+)-ATPase from rat liver plasma membranes. J. Biol. Chem. 259 (1984) 3016-3020
101. Lin S.-H., and Guidotti G. Cloning and expression of a cDNA coding for a rat liver plasma membrane ecto-ATPase. The primary structure of the ecto-ATPase is similar to that of the human biliary glycoprotein I. J. Biol. Chem. 264 (1989) 14408-14414
102. 2+-pump but an ecto-ATPase. J. Biol. Chem. 263 (1988) 12253-12258
103. 2+-ATPase in pituitary secretory granule membranes. J. Biol. Chem. 256 (1981) 12802-12810
104. Lotersztajn S., Hanoune J., and Pecker F. A high affinity calcium-stimulated magnesium-dependent ATPase in rat liver plasma membranes. Dependence on an endogenous protein activator distinct from calmodulin. J. Biol. Chem. 256 (1981) 11209-11215
105. Lotersztajn S., Epand R.M., Mallat A., and Pecker F. Inhibition by glucagon of the calcium pump in liver plasma membranes. J. Biol. Chem. 259 (1984) 8195-8201
106. Lüthje J., Schomburg A., and Ogilvie A. Demonstration of a novel ecto-enzyme on human erythrocytes, capable of degrading ADP and of inhibiting ADP-induced platelet aggregation. Eur. J. Biochem. 175 (1988) 285-289
107. 2+ nucleotide phosphohydrolases in myometrium: two ecto-enzymes. Biochim. Biophys. Acta 1070 (1991) 163-172
108. Mancilla M., Kettlun A.M., Valenzuela M.A., and Traverso-Cori A. Structural studies of two apyrases from Solanum tuberosum. Phytochemistry 23 (1984) 1397-1400
109. 24721-2474. Mancilla M., Valenzuella M.A., Anich M., Kettlun A.M., Jara O., and Traverso-Cori A. Identification of an apyrase activating protein and of calmodulin in Solanum tuberosum. Phytochemistry 26 (1987)
110. Mant M.J., and Parker K.R. Two platelet aggregation inhibitors in tsetse (Glossina) saliva with studies of roles of thrombin and citrate in in vitro platelet aggregation. Br. J. Haematol. 48 (1981) 601-608
111. Marchesi V.T., and Barnett R.J. The localization of nucleoside-phosphatase activity in different types of small blood vessels. J. Ultrastruct. Res. 10 (1963) 103-115
112. Marchesi V.T., and Barrnett R.J. The localization of nucleosidephosphatase activity in different types of small blood vessels. J. Ultrastruct. Res. 10 (1964) 103-115
113. Marcus A.J., and Safier L.B. Thromboregulation: Multicellular modulation of platelet reactivity in haemostasis and thrombosis. FASEB J. 7 (1993) 516-522
114. Marcus A.J., Safier L.B., Hajjar K.A., Ullman H.L., Islam N., Broekman M.J., and Eiroa A.M. Inhibition of platelet function by an aspirin-insensitive endothelial cell ADPase. Thromboregulation by endothelial cells. J. Clin. Invest. 88 (1991) 1690-1696
115. 2+-ATPase in plasma membrane-rich fraction of bovine parotid gland. Arch. Biochem. Biophys. 280 (1990) 362-368
116. Mazelis M. Enzymatic degradation of adenosine triphosphate to adenine by cabbage leaf preparations. Plant Physiol. 34 (1959) 153-158
117. Medzihradsky F., Cullen E.I., Lin H.L., and Bole G.G. Drug-sensitive ecto-ATPase in human leucocytes. Biochem. Pharmacol. 29 (1980) 2285-2290
118. Meghji P., Pearson J.D., and Slakey L.L. Regulation of extracellular adenosine production by ectonucleotidases of adult rat ventricular myocytes. Am. J. Physiol. 263 (1992) H40-H47
119. Meyerhof O. The origin of the reaction of harden and young in cell-free alcoholic fermentation. J. Biol. Chem. 157 (1945) 105-119
120. Miller D.L., and Weistheimer F.H. The enzymic hydrolysis of γ-phenylpropyl di- and triphosphate. J. Am. Chem. Soc. 88 (1966) 1511-1513
121. 2+-calmodulin and by oxytocin. Biochem. J. 250 (1988) 571-577
122. 2+-activated ATPase activity in smooth-muscle membranes. NADH oxidase and adenylate kinase interfere with NADH-coupled enzyme assay. Biochem. J. 250 (1988) 579-588
123. Miura Y., Hirota K., Arai Y., and Yagi K. Purification and partial characterization of adenosine diphosphatase activity in bovine aorta microsomes. Thromb. Res. 46 (1987) 685-695
124. Molnar J., and Lorand L. Studies on apyrases. Arch. Biochem. Biophys. 93 (1961) 353-363
125. Moodie F.D.L., Baum H., Butterworth P.J., and Peters T.J. Purification and characterization of bovine spleen ADPase. Eur. J. Biochem. 202 (1991) 1209-1215
126. Moulton M.P., Sabbadini R.A., Norton K.C., and Dahms A.S. Studies on the transverse tubule membrane Mg-ATPase. Lectin-induced alterations of kinetic behavior. J. Biol. Chem. 261 (1986) 12244-12251
127. 2+-pump. Biochem. Biophys. Res. Commun. 141 (1986) 979-985
128. Nagy A. Enzymatic characteristics and possible role of synaptosomal ecto-adenosine triphosphatase from mammalian brain. In: Kreutzberg, et al. (Ed). Cellular Biology of Ectoenzymes (1986), Springer-Verlag, Amsterdam 49-59
129. Nagy A., and Rosenberg M.D. Adenosine triphosphate activity at the external surface of synaptosomes. Eighth Meet. Int. Soc. Neurochem. Nottingham (1981)
130. Nagy A., Shuster T.A., and Rosenberg M.D. Adenosine triphosphatase activity at the external surface of chicken brain synaptosomes. J. Neurochem. 40 (1983) 226-234
131. Noda L. Adenylate kinase. In: Boyer P.D. (Ed). The Enzymes (1973), Academic Press, Berlin, Heidelberg 379-405
132. Novikoff A.B., and Heus M. A microsomal nucleoside diphosphatase. J. Biol. Chem. 238 (1963) 710-716
133. Novikoff P.M., Novikoff A.B., Quintana N., and Hauw J.J. Golgi-apparatus, GERL, and lysosomes of neurons in rat dorsal root ganglia studied by thick section and thin section cytochemistry. J. Cell Biol. 50 (1971) 859-886
134. 2+ transport. J. Biol. Chem. 259 (1984) 102-106
135. +-ATPase. Acta Histochem. Cytochem. 19 (1986) 601-620
136. Okamoto V.R., Moulton M.P., Runte E.M., Kent C.D., Lebherz H.G., Dahms A.S., and Sabbadini R.A. Characterization of transverse tubule membrane proteins: Tentative identification of the magnesium-ATPase. Arch. Biochem. Biophys. 237 (1985) 43-54
137. Olsson R.A., and Pearson J.D. Cardiovascular purinoceptors. Physiol. Rev. 70 (1990) 761-845
138. Paddle B.M., and Burnstock G. Release of ATP from perfused heart during coronary vasodilatation. Blood Vessels 11 (1974) 110-119
139. Paddle B.M., and Burnstock G. Release of ATP from perfused heart during coronary vasodilatation. Blood Vessels 11 (1987) 110-119
140. Papamarcaki T., and Tsolas O. Identification of ATP diphosphohydrolase activity in human term placenta using a novel assay for AMP. Molec. Cell Biochem. 97 (1990) 1-8
141. Pearson J.D. Ectonucleotidases of vascular endothelial cells: Characterization and possible physiological roles. In: Kreutzberg, et al. (Ed). Cellular Biology of Ectoenzymes (1986), Springer-Verlag Berlin, New York 16-26
142. Pearson J.D., and Gordon J.L. Vascular endothelial and smooth muscle cells in culture selectively release adenosine nucleotides. Nature (London) 281 (1979) 384-386
143. Pearson J.D., Carleton J.C., and Gordon J.L. Metabolism of adenine nucleotides by ectoenzymes of vascular endothelial and smooth-muscle cells in culture. Biochem. J. 190 (1980) 421-429
144. Pearson J.D., Coade S.B., and Cusack N.J. Characterization of ectonucleotidases on vascular smooth-muscle cells. Biochem. J. 230 (1985) 503-507
145. Pepys J., and Edwards A.M. The mast cells. Its role in health and disease. Proceedings of an International Symposium. Davos, Switzerland (1979)
146. Picher M., Côté Y.P., Béliveau R., Potier M., and Beaudoin A.R. Demonstration of a novel type of ATP-diphosphohydrolase (E.C.3.6.1.5.) in the bovine lung. J. Biol. Chem. 268 (1993) 4699-4703
147. Picher M., Béliveau R., Potier M., Savaria D., Rousseau É., and Beaudoin A.R. Demonstration of an ectoATP-diphosphohydrolase (E.C.3.6.1.5.) in non-vascular smooth muscles of the bovine trachea. Biochim. Biophys. Acta 1200 (1994) 167-174
148. Pieber M., Valenzuela M.A., Kettlun A.M., Mancilla M., Aranda E., Collados L., and Traverso-Cori A. ATPase-ADPase activities of rat placental tissue. Comp. Biochem. Biophys. 100B (1991) 281-285
149. Plaut G.W.E. An inosine diphosphatase from mammalian liver. J. Biol. Chem. 217 (1955) 235-245
150. 2+-dependent nucleoside triphosphatase from rat mesenteric small arteries. Biochim. Biophys. Acta 1067 (1991) 191-200
151. Ragazzi E., Wu S.N., Shryock J., and Belardinelli L. Electrophysiological and receptor binding studies to assess activation of the cardiac adenosine receptor by adenine nucleotides. Circ. Res. 68 (1991) 1035-1044
152. Ribeiro J.M.C. Role of saliva in blood-feeding by arthropods. Ann. Rev. Entomol. 32 (1987) 463-478
153. Ribeiro J.M.C. Vector saliva and its role in parasite transmission. Exp. Parasitol. 69 (1989) 104-106
154. Ribeiro J.M.C., and Garcia E.S. Apyrase activity in saliva and crop of Rhodnius prolixus. An. Acad. Bras. Ciênc. 51 (1979) 182
155. Ribeiro J.M.C., and Garcia E.S. The salivary and crop apyrase activity of Rhodnius prolixus. J. Insect Physiol. 26 (1980) 303-307
156. Ribeiro J.M.C., and Garcia E.S. Platelet antiaggregating activity in the salivary secretion of the blood sucking bug Rhodnius prolixus. Experimentia 37 (1981) 384-386
157. Ribeiro J.M.C., Sarkis J.J.F., Rossignol P.A., and Spielman A. Salivary apyrase of Aedes aegypti: Characterization and secretory fate. Comp. Biochem. Physiol. 79B (1984) 81-86
158. Ribeiro J.M.C., Rossignol P.A., and Spielman A. Role of mosquito saliva in blood vessel location. J. Exp. Biol. 108 (1984) 1-7
159. Ribeiro J.M.C., Sarkis J.J.F., Rossignol P.A., and Spielman A. Salivary gland apyrase determines probing time in anopheline mosquitoes. J. Insect Physiol. 31 (1985) 689-692
160. Ribeiro J.M.C., Makoul G.T., Levine J., Robinson D.R., and Spielman A. Antihemostatic, antiinflammatory and immunosuppressive properties of the salivary of a tick, Ixodes dammini. J. Exp. Med. 161 (1985) 332-344
161. Ribeiro J.M.C., Rossignol P.A., and Spielman A. Blood-finding strategy of a capillary feeding sandfly Lutzomyia longipalpis. Comp. Biochem. Physiol. 83A (1986) 683-686
162. Ribeiro J.M.C., Modi G.B., and Tesh R.B. Salivary apyrase activity of some Old World phlebotomine sandflies. Insect Biochem. 19 (1989) 409-412
163. Ribeiro J.M.C., Vaughan J.A., and Azad A.F. Characterization of the salivary apyrase of three rodent flea species. Comp. Biochem. Physiol. 95B (1990) 215-219
164. Ribeiro J.M.C., Endris T.M., and Endris R. Saliva of the soft tick, Ornithodoros moubata, contains anti-platelet and apyrase activities. Comp. Biochem. Physiol. 100A (1991) 109-112
165. Rigbi M., Levy H., Iraqui F., Teitelbaum M., Orevi M., Alajoutsijärvi A., Horowitz A., and Galun R. The saliva of the medicinal leech Hirudo medicinalis. I. Biochemical characterization of the high molecular weight fraction. Comp. Biochem. Physiol. 87B (1987) 567-573
166. Ronca-Testoni S., and Borghini F. Degradation of perfused adenine compounds up to uric acid in isolated rat heart. J. Mol. Cell. Cardiol. 14 (1982) 177-180
167. 2+ on the cell volume in isolated kidney tubules. Biochim. Biophys. Acta 274 (1972) 226-239
168. 2+-ATPase in brains of seizure prone mice. J. Neurochem. 27 (1976) 1299-1304
169. Rossignol P.A., Ribeiro J.M.C., and Spielman A. Increased intradermal probing time in sporozoite-infected mosquitoes. Am. J. Trop. Med. Hyg. 33 (1984) 17-20
170. Ryan U.U. Metabolic activity of pulmonary endothelium: Modulations of structure and function. Ann. Rev. Physiol. 48 (1986) 263-277
171. 2+-ATPase of skeletal muscle. Evidence for extracellular orientation of the chicken and rabbit enzymes. J. Biol. Chem. 266 (1991) 23490-23498
172. Sadler J.E., Beyer T.A., Oppehheimer C.L., Paulson J.C., Prieels J.I., Rearick J.I., and Hill R.L. Purification of mammalian glycosyltransferases. Meth. Enzymol. 83 (1982) 458-514
173. Sarkis J.J.F., and Salto C. Characterization of synaptosomal ATP diphosphohydrolase from the electric organ Torpedo marmorata. Brain Res. Bull 26 (1991) 871-876
174. Sarkis J.J.F., Guimaraes J.A., and Ribeiro J.M.C. Salivary apyrase of Rhodnius prolixus: Kinetics and purification. Biochem. J. 233 (1986) 885-891
175. Schadeck R.J.G., Sarkis J.J.F., Dias R.D., Araujo H.M.M., and Souza D.O.G. Synaptosomal apyrase in the hypothalamus of adult rats. Braz. J. Med. Biol. Res. 22 (1989) 303-314
176. Shubert P., Lee K., and Kreutzberg G.W. Formation and function of adenosine in the CNS. I. Release and modulatory action. Eighth Meet. Soc. Neurochem. Nottingham (1981)
177. Smith G.P., and Peters T.J. Subcellular localization and properties of adenosine diphosphatase activity in human polymorphonuclear leukocytes. Biochim. Biophys. Acta 673 (1981) 234-242
178. Smith G.P., Shah T., Webster A.D.B., and Peters T.J. Studies on the kinetic properties and subcellular localization of adenosine diphosphatase in human peripheral blood lymphocytes. Clin. Exp. Immunol. 46 (1981) 321-326
179. Smith J.J.B., Cornish R.A., and Wilkes J. Properties of a calcium-dependent apyrase in the saliva of the blood-feeding bug, Rhodnius prolixus. Experimentia 36 (1980) 898-899
180. 2+-ATPase as a membrane ecto-enzyme of human granulocytes. Inhibitors, activators and response to phagocytosis. Biochim. Biophys. Acta 512 (1978) 525-538
181. Sorensen R.G., and Mahler H.R. Localization of endogenous ATPase at the nerve terminal. J. Bioenerg. Biomembr. 14 (1982) 527-547
182. Stefanovic V., Ciesielski-Treska J., Ebel A., and Mandel P. Nucleoside triphosphate activity at the external surface of neuroblastoma cells. Brain Res. 81 (1974) 427-441
183. Stefanovic V., Ledig M., and Mandel P. Divalent cation activated ecto-nucleoside triphosphatase activity of nervous cells in tissue culture. J. Neurochem. 27 (1976) 799-805
184. Strobel R. Purification and immunochemical characterization of ectoATP-diphosphohydrolase from chicken oviduct and liver. Thesis, University of Minnesota (1992)
185. Strobel R., and Rosenberg M. Immunoaffinity chromatographic purification of chicken ectoATP diphosphohydrolase. Ann. N.Y. Acad. Sci. 671 (1992) 487-489
186. 2+-pump ATPase. J. Biochem. 108 (1990) 730-736
187. Szekely M. Purification of potato apyrase and investigation into its reaction mechanisms. Acta Chim. Acad. Sci. Hung. 1 (1951) 325-333
188. 2+-dependent ATPase in the rat parotid plasma membrane. Biochim. Biophys. Acta 945 (1988) 202-210
189. Tognoli L. Interaction of nucleoside triphosphate diphosphohydrolase from pea with a membrane protein factor. Phytochemistry 23 (1984) 515-518
190. Tognoli L., and Marrè E. Purification and characterization of a divalent cation-activated ATPase-ADPase from pea stem microsomes. Biochim. Biophys. Acta 642 (1981) 1-14
191. Torres M., Pintor J., and Miras-Portugal T. Presence of ectonucleotidases in cultured chromaffin cells: Hydrolysis of extracellular adenine nucleotides. Arch. Biochem. Biophys. 279 (1990) 37-44
192. Trams E.G., and Lauter C.J. On the sideness of plasma membrane enzymes. Biochim. Biophys. Acta 345 (1974) 180-197
193. Trams E.G., and Lauter C.J. Ecto-ATPase deficiency in glia of seizure prone mice. Nature (London) 271 (1978) 270-271
194. Traverso-Cori A., and Cori O. Splitting of the terminal phosphate group of adenosine triphosphate by potato apyrase. Biochim. Biophys. Acta 57 (1962) 158-160
195. Traverso-Cori A., Chaimovich H., and Cori O. Kinetic studies and properties of potato apyrase. Arch. Biochem. Biophys. 109 (1965) 173-184
196. Traverso-Cori A., Traverso S., and Reyes H. Different molecular forms of potato apyrase. Arch. Biochem. Biophys. 137 (1970) 133-142
197. Valenzuela M.A., Del Campo G., Marin E., and Traverso-Cori A. Effects of protein-modifying reagents on an isoenzyme of potato apyrase. Biochem. J. 133 (1973) 755-763
198. Valenzuela M.A., Kettlun A.M., Mancilla M., Calvo V., Fanta N., and Traverso-Cori A. The effect of bivalent metal ions on ATPase-ADPase activities of apyrase from Solanum tuberosum. Phytochemistry 27 (1988) 1981-1985
199. Valenzuela M.A., Lopez J., Depix M., Mancilla M., Kettlun A.M., Catalan L., Chiong M., Garrido J., and Traverso-Cori A. Comparative subcellular distribution of apyrase from animal and plant sources. Characterization and microsomal apyrase. Comp. Biochem. Physiol. 93B (1989) 509-513
200. Valenzuela M.A., Collados L., Kettlun A.M., Mancila M., Lara H., Puente J., Aranda E., Chayet L., Alvarez A., and Traverso-Cori A. Changes in apyrase activity in uterus and mammary gland during the lactogenic cycle. Comp. Biochem. Physiol. 103B (1992) 113-118
201. Vara F., and Serrano R. Purification and characterization of a membrane-bound ATP diphosphohydrolase from Cicer arietinum (chick-pea) roots. Biochem. J. 197 (1981) 637-643
202. Vasconcelos E.G., Nascimento P.S., Mierelles M.N.L., Verjovski-Almeida S., and Ferreira S.T. Characterization and localization of an ATP-diphosphohydrolase on the external surface of the tegument of Schistosoma mansoni. Mol. Biochem. Parasitol. 58 (1993) 205-214
203. Wattiaux-de-Coninck S., and Wattiaux R. Nucleoside diphosphatase activity in plasma membrane of rat liver. Biochim. Biophys. Acta 183 (1969) 118-128
204. Weiss B., and Sachs L. Differences in surface membrane ecto-ATPase and ecto-AMPase in normal and malignant cells. I. Decrease in ecto-ATPase in myeloid leukemic cells and the independent regulation of ecto-ATPase and ecto-AMPase. J. Cell Physiol. 93 (1977) 183-188
205. Welford L.A., Cusack N.J., and Hourani S.M.O. ATP analogues and the guinea-pig taenia coli: A comparison of the structure-activity relationships of ectonucleotidases with those of the P2-purinoceptor. Eur. J. Pharmacol. 129 (1986) 217-224
206. Welford L.A., Cusack N.J., and Hourani S.M.O. The structure-activity relationships of ectonucleotidases and of excitatory P2-purinoceptors: evidence that dephosphorylation of ATP analogues reduces pharmacological potency. Eur. J. Pharmacol. 141 (1987) 123-130
207. White T.D. Release of ATP from a synaptosomal preparation by elevated extracellular potassium and by veratridine. J. Neurochem. 30 (1978) 329-336
208. Wilson P.D., Rustin G.J., Smith G.P., and Peters T.J. Electron microscopic cytochemical localization of nucleoside phosphatases in normal and chronic granulocytic human neutrophils. Histochem. 13 (1981) 73-84
209. Wilson P.D., Lieberman G.E., and Peters T.J. Ultrastructural localization of adenosine diphosphatase activity in cultured aortic endothelial cells. Histochem. J. 14 (1982) 215-219
210. Yagi K., Arai Y., Kato N., Hirota K., and Miura Y. Purification of ATP diphosphohydrolase from bovine aorta microsomes. Eur. J. Biochem. 180 (1989) 509-513
211. Yagi K., Shinbo M., Hashizume M., Shimba L.S., Kurimura S., and Miura Y. ATP diphosphohydrolase is responsible for ecto-ATPase and ecto-ADPase activities in bovine aorta endothelial and smooth muscles cells. Biochem. Biophys. Res. Commun. 180 (1991) 1200-1206
212. Yagi K., Kato N., Shinbo M., Shimba L.S., and Miura Y. Purification and characterization of adenosine diphosphatase from human umbilical vessels. Chem. Pharm. Bull. 40 (1992) 2143-2146
213. Yamazaki M., and Hayaishi O. The activation of nucleoside diphosphatase by nucleoside triphosphates and its possible metabolic significance. J. Biol. Chem. 240 (1965) 2761-2762
214. Yamasaki M., and Hayaishi O. Allosteric properties of nucleoside diphosphatase and its identity with thiamine pyrophosphatase. J. Biol. Chem. 243 (1969) 2934-2942
215. Zimmermann H., Dowdall M.J., and Lane D.A. Purine salvage at the cholinergic nerve endings of the Torpedo electric organ: The central role of adenosine. Neuroscience 4 (1979) 979-993
216. Zimmermann H., Grondal E.J.M., and Keller F. Hydrolysis of ATP and formation of adenosine at the surface of cholinergic nerve endings. In: Kreutzberg, et al. (Ed). Cellular Biology of Ectoenzymes (1986), Springer-Verlag, Heidelberg 35-48